54781 Wyniki dla: „2-Chloroquinoline-5-carboxylic+acid&pageNo=48”

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Involved in craniofacial development. Acts upstream of the EDN1 pathway and is required for formation of the upper jaw equivalent, the palatoquadrate. The activity required for EDN1 pathway function differs between the first and second arches (By similarity). Associates with DIAPH1 and controls GLI1 transcriptional activity. Could be involved in normal and disease skin development. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.

Supplier: Bioss

Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2.

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Effector protein for Rho-type GTPases. Regulates actin filament reorganization via its interaction with the Arp2/3 complex. Important for efficient actin polymerization. Possible regulator of lymphocyte and platelet function. Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria.

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SEMA6A belongs to a subfamily characterized by an extracellular semaphorin domain, a transmembrane domain, and a long cytoplasmic tail. Members of this class can repel sympathetic and dorsal root ganglion axons in vitro, consistent with a traditional role as guidance signals. However, the length of the cytoplasmic tail, which includes an EVL-binding site in SEMA6A and an Src-binding site in SEMA6B, suggests that these semaphorins may also function as receptors. SEMA6A is expressed in developing neural tissue and is required for proper development of the thalamocortical projection. SEMA6A directly links the Ena/VASP and the semaphorin protein families since the SEMA6A protein is capable of selective binding to the protein EVL (Ena/VASP-like protein.

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Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.

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Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis.

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Receptor for IL27. Requires IL6ST/gp130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1-type immune responses. Also appears to be involved in innate defense mechanisms.

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This protein is associated with nerve growth. It is a major component of the motile "growth cones" that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction.

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Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH6) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis.

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Defensins are a family of microbicidal and cytotoxic peptides thought to be involved in host defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Members of the defensin family are highly similar in protein sequence and distinguished by a conserved cysteine motif. Several alpha defensin genes are clustered on chromosome 8. This gene differs from other genes of this family by an extra 83-base segment that is apparently the result of a recent duplication within the coding region. The protein encoded by this gene, defensin, alpha 4, is found in the neutrophils; it exhibits corticostatic activity and inhibits corticotropin stimulated corticosterone production. [provided by RefSeq].

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AROS-29 is suggested to have a functional role in protection against oxidative stress. The gene encoding AROS-29 is located on human chromosome 19, which consists of over 63 million bases, houses approximately 1,400 genes and is recognized for having the greatest gene density of the human chromosomes. It is the genetic home for a number of immunoglobulin superfamily members, including the killer cell and leukocyte Ig-like receptors, a number of ICAMs, the CEACAM and PSG family and Fc receptors (FcRs). Key genes for eye color and hair color also map to chromosome 19.

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RBM5 (RNA binding motif protein 5) is a nuclear SR related RNA binding protein which specifically binds poly(G) RNA homopolymers in vitro. It modulates both apoptosis and the cell cycle, and retards tumor formation.

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Estrogen and progesterone receptor are members of a family of transcription factors that are regulated by the binding of their cognate ligands. The interaction of hormone-bound estrogen receptors with estrogen responsive elements(EREs) alters transcription of ERE-containing genes. The carboxy terminal region of the estrgen receptor contains the ligand binding domain, the amino terminus serves as the transactivation domain, and the DNA binding domain is centrally located. Two forms of estrogen receptor have been identified, ER Alpha and ER Beta. ER Alpha and ER Beta have been shown to be differentially activated by various ligands. The biological response to progesterone is mediated by two distinct forms of the human progesterone receptor (hPR-A and hPR-B), which arise from alternative splicing. In most cells, hPR-B functions as a transcriptional activator of progesterone-responsive gene, whereas hPR-A function as a transcriptional inhibitor of all steroid hormone receptors.

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Latexin, a protein possessing inhibitory activity against rat carboxypeptidase A1 (CPA1) and CPA2, is expressed in a neuronal subset in the cerebral cortex and cells in other neural and non-neural tissues of rat. Although latexin also inhibits mast-cell CPA (MCCPA), the expression of latexin in rat mast cells has not previously been confirmed.

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COL20A1 is a probable collagen protein.

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EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro (PubMed:10964941).

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Binding of anti-Fx1A to Heymann nephritis antigens (HA) on rat glomerular epithelial cells (GECs) in culture leads to capping and disappearance of antigens from the cell surface. This process may contribute to the formation of glomerular subepithelial immune deposits in vivo. The authors differentially extracted GECs to determine whether HA redistribution is mediated by cytoskeletal components. Observations were made by phase-contrast and immunofluorescence microscopy on primary and passaged GECs in monolayer culture and by spectrofluorimetry on GECs in suspension.

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Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression.

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Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.

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Glypicans are glycosylphosphatidylinositol-anchored heparan sulphate proteoglycans, which are thought to modulate signalling by growth factors, including fibroblast growth factors and Wnts. Expression of glypican-4 has been reported in the mouse brain at embryonic day 7 and later stages.

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Differentiation of myogenic cells is regulated by multiple positively and negatively acting factors. One well characterized family of helix-loop-helix (HLH) proteins known to play an important role in the regulation of muscle cell development include Myo D, myogenin, Myf-5 and Myf-6 (also designated MRF-4 or herculin). Of interest, most muscle cells express either Myo D or Myf-5 in the committed state, but when induced to differentiate, all turn on expression of myogenin. Myo D transcription factors form heterodimers with products of a more widely expressed family of bHLH genes, the E family, which consists of at least three distinct genes: E2A, IF2 and HEB. Myo D-E heterodimers bind avidly to consensus (CANNTG) E box target sites that are functionally important elements in the upstream regulatory sequences of many muscle-specific terminal differentiation genes.

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Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

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Spliceosomes are multi-protein complexes that are composed of snRNPs (small nuclear ribonucleoproteins) and a variety of associated protein factors, all of which work in concert to regulate the splicing of pre-mRNA, a critical step in the post-transcriptional regulation of gene expression. CWC22 (CWC22 spliceosome-associated protein), also known as NCM, fSAPb or EIF4GL, is a 908 amino acid nuclear protein and component of the spliceosome C complex. CWC22 is associated with the spliceosome prior to catalytic steps and remains associated throughout the reaction. Belonging to the CWC22 family, CW22 contains one MI domain and a MIF4G domain. The gene encoding CWC22 maps to human chromosome 2q31.3. As the second largest human chromosome, chromosome 2 makes up approximately 8% of the human genome and contains 237 million bases encoding over 1,400 genes.

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SYAP1 (synapse-associated protein 1) is a 352 amino acid protein that is ubiquitously expressed in adult tissues. SYAP1 contains one BSD domain which is a novel domain that is present in basal transcription factors, synapse-associated proteins and several hypothetical proteins. The BSD domain is characterized by three predicted alpha helices and by conserved tryptophan and phenylalanine residues, located at the C-terminus of the domain. The gene that encodes SYAP1 in humans is located on chromosome X. Chromosome X consists of about 153 million base pairs and nearly 1,000 genes. Color blindness, hemophilia, and Duchenne muscular dystrophy are well known X chromosome-linked conditions which affect males more frequently as males carry a single X chromosome.

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Protein kinase C (PKC) zeta is a member of the PKC family of serine/threonine kinases which are involved in a variety of cellular processes such as proliferation, differentiation and secretion. Unlike the classical PKC isoenzymes which are calcium-dependent, PKC zeta exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors and cannot be activated by phorbol ester. Unlike the classical PKC isoenzymes, it has only a single zinc finger module. These structural and biochemical properties indicate that the zeta subspecies is related to, but distinct from other isoenzymes of PKC. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008].

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Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

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Src (also known as pp60src) is a non receptor Tyrosine Kinase involved in signal transduction in many biological systems and implicated in the development of human tumors. There are two critical phosphorylation sites of tyrosine on Src, tyrosine 418 and tyrosine 529 (referring to human Src sequence). The tyrosine 418 is located in the catalytic domain and is one of the autophosphorylation sites. Full catalytic activity of Src requires phosphorylation of tyrosine 418. The tyrosine 529 is located near the carboxyl terminus of Src and acts as a negative regulator, in that Src is held in the inactive form through an intramolecular interaction between the SH2 domain and the carboxyl terminus when tyrosine 529 is phosphorylated by Csk. This conformation blocks phosphorylation of tyrosine 418 at the catalytic domain, thereby preventing Src activation. When tyrosine 529 is dephosphorylated, tyrosine 418 can be maximally phosphorylated and Src becomes active. Src is a proto oncogene that may play a role in the regulation of embryonic development and cell growth. Mutations in this gene could be involved in the malignant progression of colon cancer. Immunogen: Synthetic peptide (Human) derived from the region of Src that contains tyrosine 529, based on the human sequence. The sequence is conserved in mouse (tyrosine 534), chicken (tyrosine 527) and frog (tyrosine 525).

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The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008]

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The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF32 (RING finger protein 32), also known as HSD15 or FKSG33, is a 362 amino acid cytoplasmic protein that contains one IQ domain and two RING-type zinc fingers. Highly expressed in testis with lower expression levels in ovary tissue, RNF32 is thought to play a role in spermatogenesis, specifically contributing to the growth and maturation of round spermatids. Six isoforms of RNF32 exist due to alternative splicing events.

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Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis. May be a mediator of metastasis suppression in breast carcinoma.